The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S‐peptide analogues with enhanced helical stability
The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S‐peptide analogues with enhanced helical stability
复制标题
通过掺入具有增强螺旋稳定性的 S 肽类似物来设计和生产具有增强热稳定性的半合成核糖核酸酶
DOI：
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发表时间：
1986
期刊：
影响因子：
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通讯作者：
R. L. Baldwin
中科院分区：
文献类型：
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作者：
C. Mitchinson;R. L. Baldwin
最近的研究表明，对于C肽的合成类似物（核糖核酸酶A的残基1-13），肽螺旋在水中的稳定性强烈依赖于N末端残基上的电荷。我们已经问过，在由S蛋白加上S肽类似物重构的半合成核糖核酸酶S中（1-15），肽螺旋的稳定性是否与重构核糖核酸酶S的Tm相关。已经合成了六种肽，它们含有Glu 9 → Leu、封闭的α-COO−基团（α-CONH 2）和Gln 11或Glu 11。N-末端残基是可变的;其电荷从+2（Lys）到−1（琥珀酰-Ala）不等。我们已经测量了肽螺旋的稳定性、肽对S蛋白的亲和力（通过C.D.滴定）和重构的核糖核酸酶S的热稳定性。
Recent work has shown that, with synthetic analogues of C‐peptide (residues 1–13 of ribonuclease A), the stability of the peptide helix in H2O depends strongly on the charge on the N‐terminal residue. We have asked whether, in semisynthetic ribonuclease S reconstituted from S‐protein plus an analogue of S‐peptide (1–15), the stability of the peptide helix is correlated with the Tm of the reconstituted ribonuclease S. Six peptides have been made, which contain Glu9 → Leu, a blocked α‐COO− group (CONH2), and either Gln11 or Glu11. The N‐terminal residue has been varied; its charge varies from +2 (Lys) to −1 (succinyl‐Ala). We have measured the stability of the peptide helix, the affinity of the peptide for S‐protein (by C.D. titration), and the thermal stability of the reconstituted ribonuclease S.
核糖核酸酶 S 残基 1 至 19 中最慢交换肽 NH 质子的性质和位置。
影响因子：
5.6
作者：
Kuwajima,K;Baldwin,RL
通讯作者：
Baldwin,RL